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anti-Human DLD Antikörper:
anti-Mouse (Murine) DLD Antikörper:
anti-Rat (Rattus) DLD Antikörper:
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Human Monoclonal DLD Primary Antibody für IHC (p), ELISA - ABIN560607
Chan, Qian, Diamond, Liu, Gritsenko, Monroe, Camp, Smith, Katze: Quantitative analysis of human immunodeficiency virus type 1-infected CD4+ cell proteome: dysregulated cell cycle progression and nuclear transport coincide with robust virus production. in Journal of virology 2007
Cow (Bovine) Polyclonal DLD Primary Antibody für IHC, WB - ABIN2787688
Ayanniyi, Raji, Adegoke: Prevalence of asymptomatic sacroiliac joint dysfunction and its association with leg length discrepancies in male students in selected junior secondary schools in Ibadan. in African journal of medicine and medical sciences 2008
Show all 2 Pubmed References
Pig (Porcine) Polyclonal DLD Primary Antibody für IP, ELISA - ABIN4369742
Butler, Mishur, Bhaskaran, Rea: A metabolic signature for long life in the Caenorhabditis elegans Mit mutants. in Aging cell 2013
study found that individuals infected with HBV withwith basal core promoter (BCP (zeige OPN1SW Antikörper)) double mutations (A1762T, G1764A)have lower concentrations of serum DLD than those with the wild-type BCP (zeige OPN1SW Antikörper)
Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning.
IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer.
Case Report: novel mutation in the DLD interface giving rise to DLD deficiency.
Certain DLD mutations can simultaneously induce the loss of a primary metabolic activity and the gain of a moonlighting proteolytic activity thus contributing to the metabolic derangement associated with DLD deficiency.
This molecular dynamics study proposes the structural changes that may lead to the modulation in reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase.
the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex.
the E3 binding protein (zeige PDHX Antikörper) component of the pyruvate dehydrogenase (zeige PDP Antikörper) complex appear to be a rare cause of pyruvate dehydrogenase (zeige PDP Antikörper) deficiency
Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD (zeige BRCA2 Antikörper)-binding region to valine.
DLD, malic acid, and fumaric acid can be used for development of cosmeceuticals and nutraceuticals regulating the change of skin metabolism induced by the UVB overexposure.
Data show that mitochondrial diaphorases (dihydrolipoamide dehydrogenase) in the liver contribute up to 81% to the NAD(+) pool during respiratory inhibition.
Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase.
Mice that are deficient in dihydrolipoamide dehydrogenase show increased vulnerability to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP (zeige PTPN2 Antikörper)), malonate and 3-nitropropionic acid, which have been used in models of Parkinson disease and Huntington disease (zeige HTT Antikörper)
identification and characterization of human and mouse D-lactate dehydrogenase (NAD) [D-LDH]
forms of DeltaD that have the MID can activate Notch (zeige NOTCH1 Antikörper) in trans and suppress early neurogenesis when mRNA encoding it is ectopically expressed in zebrafish embryos.
Fgfr4 (zeige FGFR4 Antikörper) mediates a signal-transduction pathway between Wnt16 (zeige WNT16 Antikörper) and Dlc, but not Dld, to regulate haematopoietic stem cells specification.
DeltaC and DeltaD interact as Notch (zeige NOTCH1 Antikörper) ligands in the zebrafish segmentation clock.
DeltaA/DeltaD regulate multiple and temporally distinct phases of notch (zeige NOTCH1 Antikörper) signaling during dopaminergic neurogenesis in zebrafish
Notch (zeige NOTCH1 Antikörper) signalling, via DeltaD, brings together ciliary length control and fluid flow hydrodynamics with transcriptional activation of laterality genes.
Several genomic regions that drive transcription in mesodermal and neuroectodermal domains have been identified. Transcription in all the neural expression domains is controlled by two regions, which are regulated by neurogenin 1 (zeige NEUROG1 Antikörper) and zash1a (zeige ASCL1A Antikörper)/b
Results suggest that Delta/D-Notch 1a (zeige NOTCH1A Antikörper) signaling is required for spinal cord oligodendrocyte specification.
DeltaD-Notch (zeige NOTCH1 Antikörper) signalling has a role in establishing the secretory fate in the zebrafish intestine
Data suggest that delta/notch (zeige NOTCH1 Antikörper)- and integrinalpha5-dependent cell polarization and fibronectin (zeige FN1 Antikörper) matrix assembly occur concomitantly and interdependently during border morphogenesis.
These findings show that the plastidial LIPOAMIDE DEHYDROGENASE, ptLPD, isoforms are critical in vivo determinants of arsenite-mediated arsenic sensitivity in Arabidopsis and possible strategic targets for increasing arsenic tolerance. [ptLPD2]
Lipoamide dehydrogenase significantly accelerates the conversion of a defined subset of NO donors to NO.
This gene encodes the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex
, dihydrolipoyl dehydrogenase, mitochondrial
, glycine cleavage system L protein
, glycine cleavage system protein L
, lipoamide dehydrogenase
, lipoamide reductase
, lipoyl dehydrogenase
, branched chain alpha-keto acid dehydrogenase complex subunit E3
, dihydrolipoamide dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex)
, dihydrolipoamide dehydrogenase
, dihydrolipoyl dehydrogenase
, protein BfmBC
, dihydrolipoamide:NAD oxidoreductase
, glycine cleavage system L-protein
, probable D-lactate dehydrogenase, mitochondrial
, after eight protein
, delta-like protein D
, dihydrolipoamide: NAD+ oxidoreductase
, Dihydrolipoyl dehydrogenase, mitochondrial